Počet záznamů: 1

Purification and characterization of nitrilase from Fusarium solani IMI196840

  1. 1.
    0348214 - MBU-M 2011 RIV GB eng J - Článek v odborném periodiku
    Vejvoda, Vojtěch - Kubáč, David - Davidová, A. - Kaplan, Ondřej - Šulc, Miroslav - Šveda, Ondřej - Chaloupková, R. - Martínková, Ludmila
    Purification and characterization of nitrilase from Fusarium solani IMI196840.
    Process Biochemistry. Roč. 45, č. 7 (2010), s. 1115-1120 ISSN 1359-5113
    Grant CEP: GA AV ČR IAA500200708; GA MŠk(CZ) LC06010; GA MŠk OC09046; GA ČR GD305/09/H008; GA MPO FT-TA5/043
    Výzkumný záměr: CEZ:AV0Z50200510
    Klíčová slova: fusarium solani * nitrilase * purification
    Kód oboru RIV: EE - Mikrobiologie, virologie
    Impakt faktor: 2.648, rok: 2010

    Nitrilase activity in Fusarium solani IMI196840 (approx. 1500Ul of culture broth) was induced by 2-cyanopyridine. The enzyme was purified by a factor of 20.3 at a yield of 26.9 percent. According to gel filtration, the holoenzyme was an approx. 550-kDa homooligomer consisting of subunits with a molecular weight of approximately 40 kDa, as determined by SDS-PAGE. Mass spectrometry analysis of the tryptic fragments suggested a high similarity of this enzyme to the hypothetical CN hydrolases from Aspergillus oryzae, Gibberella zeae, Gibberella moniliformis and Nectria haematococca. Circular dichroism and fluorescence spectra indicated that secondary structure content and overall tertiary structure, respectively, were almost identical in nitrilases from F. solani IMI196840 and F. solani O1
    Trvalý link: http://hdl.handle.net/11104/0188801